Journal article

Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops

DM Hatters, CE MacPhee, LJ Lawrence, WH Sawyer, GJ Howlett

Biochemistry | AMER CHEMICAL SOC | Published : 2000

Abstract

Human apolipoprotein C-II (apoC-II) self-associates in solution to form aggregates with the characteristics of amyloid including red-green birefringence in the presence of Congo Red under cross-polarized light, increased fluorescence in the presence of thioflavin T, and a fibrous structure when examined by electron microscopy. ApoC-II was expressed and purified from Escherichia coli and rapidly exchanged from 5 M guanidine hydrochloride into 100 mM sodium phosphate, pH 7.4, to a final concentration of 0.3 mg/mL. This apoC-II was initially soluble, eluting as low molecular weight species in gel filtration experiments using Sephadex G-50. Circular dichroism (CD) spectroscopy indicated predomin..

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University of Melbourne Researchers